Lipase - Revision history

Michal Harel at 08:33, 15 January 2023

Michal Harel — Sun, 15 Jan 2023 08:33:09 GMT

←Older revision		Revision as of 08:33, 15 January 2023
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	[[Image:Picture 1.png]]		[[Image:Picture 1.png]]
	Further breakdown ultimately results in 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>. An in depth discussion of the mechanism can be found in the Lipase Catalytic Mechanism section. The determination of the structure and function of lipase was a gradual process. Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846. However, it wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>. In recent years, determination of the crystal structure of pancreatic lipase has become the primary focus as many scientists have worked to further this.<br />		Further breakdown ultimately results in 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>. An in depth discussion of the mechanism can be found in the Lipase Catalytic Mechanism section. The determination of the structure and function of lipase was a gradual process. Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846. However, it wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>. In recent years, determination of the crystal structure of pancreatic lipase has become the primary focus as many scientists have worked to further this.<br />
		+
	==See also==		==See also==
	* [[Molecular Playground/Pancreatic Lipase]]<br />		* [[Molecular Playground/Pancreatic Lipase]]<br />
Line 20:		Line 21:
	* [[Monoglyceride lipase]]<br />		* [[Monoglyceride lipase]]<br />
	* [[Human gastric lipase]]<br />		* [[Human gastric lipase]]<br />
		+	* [[Lipoprotein Lipase (LPL) complexed with GPIHBP1]]<br />
	* [[Lipase (Hebrew)]]<br />		* [[Lipase (Hebrew)]]<br />
	* [[Lipid metabolism]]		* [[Lipid metabolism]]

Alexander Berchansky at 09:35, 25 December 2019

Alexander Berchansky — Wed, 25 Dec 2019 09:35:01 GMT

←Older revision		Revision as of 09:35, 25 December 2019
Line 13:		Line 13:
	[[Image:Picture 1.png]]		[[Image:Picture 1.png]]
	Further breakdown ultimately results in 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>. An in depth discussion of the mechanism can be found in the Lipase Catalytic Mechanism section. The determination of the structure and function of lipase was a gradual process. Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846. However, it wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>. In recent years, determination of the crystal structure of pancreatic lipase has become the primary focus as many scientists have worked to further this.<br />		Further breakdown ultimately results in 2-monoacylglycerols and free fatty acids <ref name= "A cross-linked complex between horse pancreatic lipase and colipase">[http://www.sciencedirect.com/science/article/pii/0014579389815923] A cross-linked complex between horse pancreatic lipase and colipase</ref>. An in depth discussion of the mechanism can be found in the Lipase Catalytic Mechanism section. The determination of the structure and function of lipase was a gradual process. Lipase activity was first demonstrated in the pancreas by Claude Bernard in 1846. However, it wasn't until 1955 that Mattson and Beck demonstrated a high-specificity of pancreatic lipase for triglyceride primary esters <ref name= "History of Lipids">[http://www.cyberlipid.org/history/history1.htm] History of Lipids</ref>. In recent years, determination of the crystal structure of pancreatic lipase has become the primary focus as many scientists have worked to further this.<br />
-	==~~'''~~See also~~'''~~==~~<br />~~	+	==See also==
	* [[Molecular Playground/Pancreatic Lipase]]<br />		* [[Molecular Playground/Pancreatic Lipase]]<br />
	* [[Lipase lid morph]]<br />		* [[Lipase lid morph]]<br />

Alexander Berchansky at 11:09, 19 December 2019

Alexander Berchansky — Thu, 19 Dec 2019 11:09:32 GMT

←Older revision		Revision as of 11:09, 19 December 2019
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	* [[Human gastric lipase]]<br />		* [[Human gastric lipase]]<br />
	* [[Lipase (Hebrew)]]<br />		* [[Lipase (Hebrew)]]<br />
		+	* [[Lipid metabolism]]

	== '''Structure''' ==		== '''Structure''' ==

Alexander Berchansky at 11:00, 19 December 2019

Alexander Berchansky — Thu, 19 Dec 2019 11:00:19 GMT

←Older revision		Revision as of 11:00, 19 December 2019
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	* The '''bile salt-stimulated lipase''' (BSSL) is found in breast milk.<br />		* The '''bile salt-stimulated lipase''' (BSSL) is found in breast milk.<br />
	* The '''hormone-sensitive lipase''' (LIPE) hydrolyzes a variety of esters. For details see [[Hormone sensitive lipase]].<br />		* The '''hormone-sensitive lipase''' (LIPE) hydrolyzes a variety of esters. For details see [[Hormone sensitive lipase]].<br />
-	* '''Monoacylglycerol lipase''' (MAGL) hydrolyzes intracellular triglycerides to fatty acid and glycerol. MAGL functions together with LIPE. For details see [[Monoglyceride lipase]].~~br/>~~	+	* '''Monoacylglycerol lipase''' (MAGL) hydrolyzes intracellular triglycerides to fatty acid and glycerol. MAGL functions together with LIPE. For details see [[Monoglyceride lipase]].

	The reaction catalyzed by the enzyme is shown below.		The reaction catalyzed by the enzyme is shown below.

Michal Harel at 09:58, 22 October 2019

Michal Harel — Tue, 22 Oct 2019 09:58:46 GMT

←Older revision		Revision as of 09:58, 22 October 2019
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	</StructureSection>		</StructureSection>

-	== 3D Structures of Lipase ==
-
-	Updated on {{REVISIONDAY2}}-{{MONTHNAME\|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-	{{#tree:id=OrganizedByTopic\|openlevels=0\|
-
-	*Eukaryote lipase:
-
-	**[[1hpl]] – hLip – horse <br />
-	**[[1hlg]] – hLip – human - gastric<br />
-	**[[1jmy]] – hBSSL <br />
-	**[[1akn]] – cBSSL – cattle <br />
-	**[[2bce]] - cBSSL (mutant) <br />
-	**[[1f6w]] - cBSSL – catalytic domain<br />
-	**[[3o0d]] – Lip – ''Yarrowia lipolytica''<br />
-	**[[4jei]] – YlLip (mutant)<br />
-	**[[1gpl]] – Lip – Guinea pig<br />
-	**[[3zpx]] – Lip – ''Ustilago maydis''<br />
-	**[[6a0w]] – Lip catalytic domain – bread mold<br />
-	**[[4zrd]], [[4zre]] – Lip1 (mutant) – dandruff fungus<br />
-
-	*Prokaryote lipase:
-
-	**[[1llf]] – Lip – ''Candida cylindracea''<br />
-	**[[3g7n]] – Lip - ''Penicillium expansum''<br />
-	**[[1tia]] - Lip – ''Penicillium camemberti''<br />
-	**[[2hih]] – Lip – ''Staphylococcus hyicus''<br />
-	**[[2fx5]] – Lip – ''Pseudomonas mendocina''<br />
-	**[[1yzf]] – Lip – ''Enterococcus faecalis''<br />
-	**[[1dt3]], [[1dt5]], [[1dte]], [[1du4]], [[1ein]], [[1tib]], [[4dyh]], [[4ea6]], [[4flf]], [[4gbg]], [[4gwl]], [[4zgb]], [[6hw1]] - TlLip - ''Thermomyces lanuginose''<br />
-	**[[5ap9]] – TlLip (mutant)<br />
-	**[[1jfr]] – Lip – ''Streptomyces exfoliates''<br />
-	**[[5mal]] – Lip – ''Streptomyces rimosus''<br />
-	**[[2lip]] – BcLip – open state<br />
-	**[[1cvl]] – Lip – ''Chromobacterium viscosum''<br />
-	**[[1tic]] - Lip – ''Rhizopus oryzae''<br />
-	**[[3tgl]], [[4tgl]], [[1tgl]], [[6qpp]] – RmLip – ''Rhyzomucor miehei''<br />
-	**[[6qpr]] – RmLip (mutant)<br />
-	**[[2zvd]] – PsLip - ''Pseudomonas sp.'' – open state<br />
-	**[[2z8x]] - PsLip – extracellular<br />
-	**[[5xpx]] – PsLip residues 1-388<br />
-	**[[2zj6]], [[2zj7]] – PsLip (mutant) <br />
-	**[[2z8z]] – PsLip(mutant) – closed state<br />
-	**[[3lip]], [[3a6z]] - Lip - ''Pseudomonas cepacia'' – open state<br />
-	**[[1qge]], [[1tah]] – Lip – ''Pseudomonas glumae''<br />
-	**[[2w22]], [[6a12]] – GtLip – ''Geobacillus thermocatenulatus''<br />
-	**[[5ce5]] – GtLip (mutant)<br />
-	**[[1ji3]], [[1ku0]], [[4fmp]], [[4x6u]] – BstLip – ''Bacillus stearothermophilus''<br />
-	**[[4x71]], [[4x7b]], [[4x85]], [[6s3g]], [[6s3j]], [[6s3v]], [[6fz1]], [[6fz7]], [[6fz8]], [[6fz9]], [[6fza]], [[6fzc]], [[6fzd]] – BstLip (mutant)<br />
-	**[[1ah7]] - Lip – ''Bacillus cereus''<br />
-	**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />
-	**[[2z5g]], [[2dsn]] – GzLip T1 – ''Geobacillus zalihae''<br />
-	**[[3umj]] – GzLip (mutant)<br />
-	**[[3p94]] – Lip – ''Parabacteroides distasonis''<br />
-	**[[3ngm]] – Lip – ''Gibberella zeae''<br />
-	**[[3auk]] - Lip – ''Geobacillus''<br />
-	**[[3uue]], [[3uuf]] – Lip – ''Malassezia globosa''<br />
-	**[[4hs9]] – Lip – ''Proteus mirabilis''<br />
-	**[[4opm]] – Lip – ''Acinetobacter baumannii''<br />
-	**[[5ah0]] – Lip – ''Pelosinus fermentans''<br />
-	**[[5ah1]] – Lip – ''Clostridium botulinum''<br />
-	**[[5ch8]] – Lip (mutant) – ''Penicillium cyclopium''<br />
-
-	*Bacterial lipase A
-
-	**[[3guu]] – CaLipA – ''Candida Antarctica''<br />
-	**[[2veo]] – CaLipA – closed state<br />
-	**[[2qua]], [[2qub]] – SmLipA – ''Serratia marcescens''<br />
-	**[[2qxt]], [[2qxu]], [[1isp]], [[1i6w]], [[5ct4]], [[5ct5]], [[5ct6]], [[5cri]] - BsLipA – ''Bacillus subtilis''<br />
-	**[[3d2a]], [[3d2b]], [[3d2c]], [[1t2n]], [[1t4m]], [[5ct8]], [[5ct9]], [[5cta]], [[5cur]], [[3qzu]], [[3qmm]] - BsLipA (mutant) <br />
-	**[[1r4z]] – BsLipA+Rc-IPG-phosphonate<br />
-	**[[1r50]] – BsLipA +Sc-IPG-phosphonate<br />
-
-	*Bacterial lipase B
-
-	**[[4zv7]], [[3w9b]], [[5a6v]], [[5a71]], [[4k6g]], [[1tca]], [[1tcb]], [[1tcc]], [[1lbs]], [[1lbt]] – CaLipB <br />
-	**[[3icv]], [[4k5q]], [[5k6h]], [[5k6k]] – CaLipB (mutant) <br />
-	**[[5gv5]] - CaLipB + phosphonate<br />
-	**[[3icw]] – CaLipB (mutant) + phosphonate<br />
-	**[[5x7k]] – SmLipB NBD <br />
-	**[[6isp]], [[6isq]], [[6isr]] – LipB (mutant) – ''Pseudozyma antarctica''<br />
-	**[[6idy]] - AfLipB - ''Aspergillus fumigatus''<br />
-
-	*Bacterial lipase C
-
-	**[[5nen]] – SmLipC residues 1-443 <br />
-
-	*Lipase/colipase complexes. The colipase is a co-enzyme whose binding to lipase optimizes the enzymatic activity
-
-	**[[1n8s]] – hLip+colipase II<br />
-	**[[1eth]], [[1lpa]] - pLip+colipase II - pig<br />
-
-	*Hormone-sensitive-lipases (LIPE) hydrolyze the first fatty acid of the triacylglycerol substrate
-
-	**[[3k6k]] – EstE7(LIPE) – metagenome library<br />
-	**[[3fak]], [[3dnm]] – EstE5(LIPE) – metagenome library<br />
-	**[[1evq]] – AaEst2(LIPE) – ''Alicyclobacillus acidocaldarius''<br />
-	**[[1u4n]] – AaEst2(LIPE) (mutant) <br />
-
-	*Putative lipases; Proteins with unknown function but structural similarity to lipase obtained in structural genomics projects.
-
-	**[[2rau]] - Lip – ''Sulfolobus solfataricus''<br />
-	**[[3bxp]], [[3d3n]] - Lip – ''Lactobacillus plantarum''<br />
-	**[[3e0x]] - Lip – ''Clostridium acetobutylicum''<br />
-	**[[1z8h]] – Lip – ''Nostoc sp.'' PCC 712<br />
-	**[[1vj3]] - Lip – ''Nostoc sp.'' <br />
-	**[[3bzw]] – Lip - ''Bacteroides thetaiotaomicron''<br />
-	**[[2pbl]] – Lip - ''Silicibacter''
-
-	*Lipase + inhibitors
-
-	**[[3l1h]] – EstE5(LIPE)+FeCl3 – noninvasive inhibitor<br />
-	**[[3l1i]], [[3l1j]] - EstE5(LIPE)+CuSO4 – noninvasive inhibitor<br />
-	**[[3lij]] - EstE5(LIPE)+ZnSO4– noninvasive inhibitor<br />
-	**[[3h18]], [[3h17]] - EstE5 (LIPE)+PMSF <br />
-	**[[3h19]], [[3h1b]], [[3h1a]] – EstE5 (LIPE)+methyl alcohol<br />
-	**[[3h1a]] – EstE5 SLIPE)+ethyl alcohol<br />
-	**[[3h19]] – EstE5 SLIPE)+isopropyl alcohol<br />
-	**[[3g9t]], [[3g9u]] - EstE5 (HSLIPE)+p-nitrophenyl butyrate<br />
-	**[[3g9z]] - EstE5 (LIPE) +p-nitrophenyl caprylate<br />
-	**[[2nw6]] – BcLip+ S inhibitor <br />
-	**[[4lip]], [[5lip]], [[1r4z]], [[1r50]] – BcLip+ Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate<br />
-	**[[1k8q]] - Lip+phosphonate – dog <br />
-	**[[1ex9]] – Lip+Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate – ''Pseudomonas aeruginosa'' <br />
-	**[[5tgl]] – RmLip+N-hexyl-phosphonate <br />
-	**[[1lpb]] – pLip + colipase+C11 alkyl phosphonate <br />
-	**[[3a70]] – PsLip+diethyl phosphate<br />
-	**[[4glb]] – TlLip + nitrobenzaldehyde<br />
-	**[[4kjx]] - TlLip + nitrobenzaldehyde + lauric acid<br />
-	**[[4n8s]] - TlLip + nitrobenzaldehyde + ethylacetoacetate<br />
-	**[[4s0x]] – TlLip + lauric acid<br />
-
-	*Lipase conjugated with analogs to its reaction intermediates
-
-	**[[1qz3]] – EaEst2(mutant) (LIPE)+hexadecanesulfonate <br />
-
-	*Bile-salt activated lipase
-
-	**[[6h0t]] – hBAL (mutant) <br />
-	**[[6h0v]], [[6h18]], [[6h19]], [[6h1a]] – hBAL (mutant) + nerve agent<br />
-	**[[1aql]] – bBAL+taurocholate - bovine<br />
-
-	*Monoacylglycerol lipase
-
-	**[[3hju]], [[3jw8]] - hMAGL <BR />
-	**[[3jwe]], [[3pe6]], [[4uuq]], [[6ax1]], [[6bq0]] – hMAGL + inhibitor<br />
-	**[[4uuq]] - hMAGLip + SAR <br />
-	**[[5zun]] – hMAGL (mutant) + inhibitor<br />
-	**[[3rm3]], [[4lhe]], [[5xks]] - BaMAGL – ''Bacillus'' <BR />
-	**[[3rli]] – BaMAGL + PMSF<br />
-	**[[4ke7]], [[4ke8]], [[4ke9]] – BaMAGL + ligand<br />
-	**[[4ke6]], [[4kea]] – BaMAGL (mutant) + ligand<br />
-	**[[4zwn]] – yMAGL – yeast<br />
-	**[[4zxf]] – yMAGLip + substrate analog<br />
-	**[[6eic]] – MAGLip – ''Mycobacterium tuberculosis''<br />
-	**[[5xk2]] – MAGLip – ''Aespergillus oryzae''<br />
-
-	*Lipase with substrate bound at active site
-
-	**[[2zyh]] – AfLip (mutant)+fatty acid – ''Archaeoglobus fulgidus''<br />
-	**[[2zyi]], [[2zyr]], [[2zys]] - AfLip+fatty acid+ ion <br />
-	**[[1gt6]], [[4ghw]], [[4gi1]] – TlLip+ fatty acid - lipid ligand<br />
-
-	*Lipase conjugated to transition-state analogs showing the binding mode of the enzyme catalysis
-
-	**[[1ys1]] – BhLip+hexylphosphonic acid (R) 2-methyl-3-phenylpropyl ester <br />
-	**[[1ys2]] – BhLip+hexylphosphonic acid (S) 2-methyl-3-phenylpropyl ester<br />
-	**[[1hqd]] – Lip+1-phenoxy-2-acrtoxy butane – ''Pseudomonas cepacia'' <br />
-
-	*Lipase+lipase chaperone
-
-	**[[2es4]] – Lip+lipase chaperone C-terminal - ''Burkholderia glumae''
-
-	*Lipase 2 or esterase/lipase
-
-	**[[3v9a]],[[3g9t]], [[3g9u]], [[3g9z]], [[3h19]], [[3h1a]], [[3h1b]], [[3l1h]], [[3l1i]], [[3l1j]], [[3fak]], [[3h17]], [[3h18]], [[3dnm]], [[3k6k]] - E/L - uncultured bacteria<br />
-	**[[3w9b]] - CaE/L <br />
-	**[[4v2i]] - E/L - ''Thalassospira''<br />
-	**[[4n5h]] - LrE/L (mutant) - ''Lactobacillus rhamnosus''<br />
-	**[[4n5i]] - LrE/L + inhibitor <br />
-	**[[4ouk]] - LrE/L (mutant) + inhibitor <br />
-	**[[4bzz]], [[4bzw]] - LpE/L <br />
-	**[[6gup]] - AfE/L <br />
-	**[[1lgy]] – Lip2 – ''Rhizopus niveus''<br />
-	**[[1gz7]] - CrLip2 <br />
-	**[[4jei]] – Lip2 – ''Yarrowia lipolytica''<br />
-	**[[1thg]] – Lip2 – ''Geotrichum candidum''<br />
-	}}
	==References==		==References==
	<references />		<references />

	[[Category:Topic Page]]		[[Category:Topic Page]]

Michal Harel at 09:54, 22 October 2019

Michal Harel — Tue, 22 Oct 2019 09:54:08 GMT

←Older revision		Revision as of 09:54, 22 October 2019
Line 60:		Line 60:
	== '''Clinical Significance''' ==		== '''Clinical Significance''' ==
	Pancreatic lipase is secreted into the duodenum through the duct system of the pancreas. In a healthy individual, it is at very low concentration in serum. Under extreme disruption of pancreatic function, such as pancreatitis or pancreatic cancer, the pancreas may begin to digest itself and release pancreatic enzymes including pancreatic lipase into serum. Measurement of serum concentration of pancreatic lipase can therefore aid in diagnosis of acute pancreatitis.<ref>"Pancreatic lipase". Wikipedia: The Free Encyclopedia. 7 Nov 2011 [http://en.wikipedia.org/wiki/Pancreatic_lipase]</ref>. Due to lipase's activity in the digestion and absorption of fat, there has been a growing market for lipase inhibitors for weight loss pharmaceuticals. The most popular is Orlistat (or Xenical®) which is a natural product from ''Streptomyces toxytricini'' and is the hydrogenation product of lipostation- an irreversible lipase inhibitor. This inhibitor also acts by binding Ser152, producing an ester which hydrolyzes so slow that it is practically irreversible <ref>Kordik, C., Reitz, A. "Pharmacological Treatment of Obesity: Therapeutic Strategies" Journal of Medicinal Chemistry, 1999 (42).</ref>.		Pancreatic lipase is secreted into the duodenum through the duct system of the pancreas. In a healthy individual, it is at very low concentration in serum. Under extreme disruption of pancreatic function, such as pancreatitis or pancreatic cancer, the pancreas may begin to digest itself and release pancreatic enzymes including pancreatic lipase into serum. Measurement of serum concentration of pancreatic lipase can therefore aid in diagnosis of acute pancreatitis.<ref>"Pancreatic lipase". Wikipedia: The Free Encyclopedia. 7 Nov 2011 [http://en.wikipedia.org/wiki/Pancreatic_lipase]</ref>. Due to lipase's activity in the digestion and absorption of fat, there has been a growing market for lipase inhibitors for weight loss pharmaceuticals. The most popular is Orlistat (or Xenical®) which is a natural product from ''Streptomyces toxytricini'' and is the hydrogenation product of lipostation- an irreversible lipase inhibitor. This inhibitor also acts by binding Ser152, producing an ester which hydrolyzes so slow that it is practically irreversible <ref>Kordik, C., Reitz, A. "Pharmacological Treatment of Obesity: Therapeutic Strategies" Journal of Medicinal Chemistry, 1999 (42).</ref>.
		+
		+	== 3D Structures of Lipase ==
		+	[[Lipase 3D Structures]]

	</StructureSection>		</StructureSection>
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	**[[2fx5]] – Lip – ''Pseudomonas mendocina''<br />		**[[2fx5]] – Lip – ''Pseudomonas mendocina''<br />
	**[[1yzf]] – Lip – ''Enterococcus faecalis''<br />		**[[1yzf]] – Lip – ''Enterococcus faecalis''<br />
-	**[[1dt3]], [[1dt5]], [[1dte]], [[1du4]], [[1ein]], [[1tib]], [[4dyh]], [[4ea6]], [[4flf]], [[4gbg]], [[4gwl]], [[4zgb]] - TlLip - ''Thermomyces lanuginose''<br />	+	**[[1dt3]], [[1dt5]], [[1dte]], [[1du4]], [[1ein]], [[1tib]], [[4dyh]], [[4ea6]], [[4flf]], [[4gbg]], [[4gwl]], [[4zgb]], [[6hw1]] - TlLip - ''Thermomyces lanuginose''<br />
	**[[5ap9]] – TlLip (mutant)<br />		**[[5ap9]] – TlLip (mutant)<br />
	**[[1jfr]] – Lip – ''Streptomyces exfoliates''<br />		**[[1jfr]] – Lip – ''Streptomyces exfoliates''<br />
	**[[5mal]] – Lip – ''Streptomyces rimosus''<br />		**[[5mal]] – Lip – ''Streptomyces rimosus''<br />
-	**[[1oil]] – BcLip - ''Burkholderia cepacia''<br />
	**[[2lip]] – BcLip – open state<br />		**[[2lip]] – BcLip – open state<br />
	**[[1cvl]] – Lip – ''Chromobacterium viscosum''<br />		**[[1cvl]] – Lip – ''Chromobacterium viscosum''<br />
	**[[1tic]] - Lip – ''Rhizopus oryzae''<br />		**[[1tic]] - Lip – ''Rhizopus oryzae''<br />
-	**[[3tgl]], [[4tgl]], [[1tgl]] – RmLip – ''Rhyzomucor miehei''<br />	+	**[[3tgl]], [[4tgl]], [[1tgl]], [[6qpp]] – RmLip – ''Rhyzomucor miehei''<br />
		+	**[[6qpr]] – RmLip (mutant)<br />
	**[[2zvd]] – PsLip - ''Pseudomonas sp.'' – open state<br />		**[[2zvd]] – PsLip - ''Pseudomonas sp.'' – open state<br />
	**[[2z8x]] - PsLip – extracellular<br />		**[[2z8x]] - PsLip – extracellular<br />
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	**[[5ce5]] – GtLip (mutant)<br />		**[[5ce5]] – GtLip (mutant)<br />
	**[[1ji3]], [[1ku0]], [[4fmp]], [[4x6u]] – BstLip – ''Bacillus stearothermophilus''<br />		**[[1ji3]], [[1ku0]], [[4fmp]], [[4x6u]] – BstLip – ''Bacillus stearothermophilus''<br />
-	**[[4x71]], [[4x7b]], [[4x85]] – BstLip (mutant)<br />	+	**[[4x71]], [[4x7b]], [[4x85]], [[6s3g]], [[6s3j]], [[6s3v]], [[6fz1]], [[6fz7]], [[6fz8]], [[6fz9]], [[6fza]], [[6fzc]], [[6fzd]] – BstLip (mutant)<br />
	**[[1ah7]] - Lip – ''Bacillus cereus''<br />		**[[1ah7]] - Lip – ''Bacillus cereus''<br />
	**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />		**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />
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	**[[3guu]] – CaLipA – ''Candida Antarctica''<br />		**[[3guu]] – CaLipA – ''Candida Antarctica''<br />
	**[[2veo]] – CaLipA – closed state<br />		**[[2veo]] – CaLipA – closed state<br />
-	**[[2qua]], 2qub]] – SmLipA – ''Serratia marcescens''<br />	+	**[[2qua]], [[2qub]] – SmLipA – ''Serratia marcescens''<br />
-	**[[2qxt]], 2qxu]], 1isp]], 1i6w]], [[5ct4]], [5ct5]], [[5ct6]], [[5cri]] - BsLipA – ''Bacillus subtilis''<br />	+	**[[2qxt]], [[2qxu]], [[1isp]], [[1i6w]], [[5ct4]], [[5ct5]], [[5ct6]], [[5cri]] - BsLipA – ''Bacillus subtilis''<br />
-	**[[3d2a]], 3d2b]], 3d2c]], 1t2n]], 1t4m]], [[5ct8]], [[5ct9]], [[5cta]], [[5cur]], [[3qzu]], [[3qmm]] - BsLipA (mutant) <br />	+	**[[3d2a]], [[3d2b]], [[3d2c]], [[1t2n]], [[1t4m]], [[5ct8]], [[5ct9]], [[5cta]], [[5cur]], [[3qzu]], [[3qmm]] - BsLipA (mutant) <br />
	**[[1r4z]] – BsLipA+Rc-IPG-phosphonate<br />		**[[1r4z]] – BsLipA+Rc-IPG-phosphonate<br />
	**[[1r50]] – BsLipA +Sc-IPG-phosphonate<br />		**[[1r50]] – BsLipA +Sc-IPG-phosphonate<br />
Line 141:		Line 144:
	**[[5gv5]] - CaLipB + phosphonate<br />		**[[5gv5]] - CaLipB + phosphonate<br />
	**[[3icw]] – CaLipB (mutant) + phosphonate<br />		**[[3icw]] – CaLipB (mutant) + phosphonate<br />
-	**[[5x7k]] – SmLipB NBD <br /><br />	+	**[[5x7k]] – SmLipB NBD <br />
		+	**[[6isp]], [[6isq]], [[6isr]] – LipB (mutant) – ''Pseudozyma antarctica''<br />
		+	**[[6idy]] - AfLipB - ''Aspergillus fumigatus''<br />

	*Bacterial lipase C		*Bacterial lipase C
Line 196:		Line 201:
	**[[1qz3]] – EaEst2(mutant) (LIPE)+hexadecanesulfonate <br />		**[[1qz3]] – EaEst2(mutant) (LIPE)+hexadecanesulfonate <br />

-	*~~Lipase showing bile~~-salt ~~binding site~~	+	*Bile-salt activated lipase

-	**[[1aql]] – ~~cBSSL~~+taurocholate <br />	+	**[[6h0t]] – hBAL (mutant) <br />
		+	**[[6h0v]], [[6h18]], [[6h19]], [[6h1a]] – hBAL (mutant) + nerve agent<br />
		+	**[[1aql]] – bBAL+taurocholate - bovine<br />

	*Monoacylglycerol lipase		*Monoacylglycerol lipase

-	**[[3rm3]], [[4lhe]], [[5xks]] - BaMAGL – ''Bacillus'' <BR />
	**[[3hju]], [[3jw8]] - hMAGL <BR />		**[[3hju]], [[3jw8]] - hMAGL <BR />
		+	**[[3jwe]], [[3pe6]], [[4uuq]], [[6ax1]], [[6bq0]] – hMAGL + inhibitor<br />
		+	**[[4uuq]] - hMAGLip + SAR <br />
		+	**[[5zun]] – hMAGL (mutant) + inhibitor<br />
		+	**[[3rm3]], [[4lhe]], [[5xks]] - BaMAGL – ''Bacillus'' <BR />
	**[[3rli]] – BaMAGL + PMSF<br />		**[[3rli]] – BaMAGL + PMSF<br />
	**[[4ke7]], [[4ke8]], [[4ke9]] – BaMAGL + ligand<br />		**[[4ke7]], [[4ke8]], [[4ke9]] – BaMAGL + ligand<br />
	**[[4ke6]], [[4kea]] – BaMAGL (mutant) + ligand<br />		**[[4ke6]], [[4kea]] – BaMAGL (mutant) + ligand<br />
-	**[[3jwe]], [[3pe6]], [[4uuq]], [[6ax1]], [[6bq0]] – hMAGL + inhibitor<br />
	**[[4zwn]] – yMAGL – yeast<br />		**[[4zwn]] – yMAGL – yeast<br />
	**[[4zxf]] – yMAGLip + substrate analog<br />		**[[4zxf]] – yMAGLip + substrate analog<br />
Line 238:		Line 247:
	**[[4ouk]] - LrE/L (mutant) + inhibitor <br />		**[[4ouk]] - LrE/L (mutant) + inhibitor <br />
	**[[4bzz]], [[4bzw]] - LpE/L <br />		**[[4bzz]], [[4bzw]] - LpE/L <br />
-	**[[6gup]] - E/L ~~- ''Aspergillus fumigatus''~~<br />	+	**[[6gup]] - AfE/L <br />
	**[[1lgy]] – Lip2 – ''Rhizopus niveus''<br />		**[[1lgy]] – Lip2 – ''Rhizopus niveus''<br />
	**[[1gz7]] - CrLip2 <br />		**[[1gz7]] - CrLip2 <br />

Joel L. Sussman at 08:29, 10 October 2019

Joel L. Sussman — Thu, 10 Oct 2019 08:29:49 GMT

←Older revision		Revision as of 08:29, 10 October 2019
Line 80:		Line 80:
	**[[1gpl]] – Lip – Guinea pig<br />		**[[1gpl]] – Lip – Guinea pig<br />
	**[[3zpx]] – Lip – ''Ustilago maydis''<br />		**[[3zpx]] – Lip – ''Ustilago maydis''<br />
-	**[[~~4l3w~~]] – Lip catalytic domain – bread mold<br />	+	**[[6a0w]] – Lip catalytic domain – bread mold<br />
	**[[4zrd]], [[4zre]] – Lip1 (mutant) – dandruff fungus<br />		**[[4zrd]], [[4zre]] – Lip1 (mutant) – dandruff fungus<br />

Michal Harel at 09:38, 20 December 2018

Michal Harel — Thu, 20 Dec 2018 09:38:26 GMT

←Older revision		Revision as of 09:38, 20 December 2018
Line 85:		Line 85:
	*Prokaryote lipase:		*Prokaryote lipase:

-	**[[3guu]], [[1lbs]], [[1lbt]], [[1tca]], [[1tcb]], [[1tcc]] – CaLipA – ''Candida antarctica''<br />
-	**[[2veo]] – CaLipA – closed state<br />
-	**[[4k6g]], [[4zv7]], [[3w9b]], [[5a6v]], [[5a71]] – CaLipB<br />
-	**[[3icv]], [[4k5q]], [[4k6h]], [[4k6k]] – CaLipB (mutant) <br />
	**[[1llf]] – Lip – ''Candida cylindracea''<br />		**[[1llf]] – Lip – ''Candida cylindracea''<br />
	**[[3g7n]] – Lip - ''Penicillium expansum''<br />		**[[3g7n]] – Lip - ''Penicillium expansum''<br />
	**[[1tia]] - Lip – ''Penicillium camemberti''<br />		**[[1tia]] - Lip – ''Penicillium camemberti''<br />
-	**[[2qua]], [[2qub]] – SmLipA – ''Serratia marcescens''<br />
-	**[[5x7k]] – SmLipB NBD <br />
-	**[[5nen]] – SmLipC residues 1-443 <br />
	**[[2hih]] – Lip – ''Staphylococcus hyicus''<br />		**[[2hih]] – Lip – ''Staphylococcus hyicus''<br />
	**[[2fx5]] – Lip – ''Pseudomonas mendocina''<br />		**[[2fx5]] – Lip – ''Pseudomonas mendocina''<br />
Line 105:		Line 98:
	**[[2lip]] – BcLip – open state<br />		**[[2lip]] – BcLip – open state<br />
	**[[1cvl]] – Lip – ''Chromobacterium viscosum''<br />		**[[1cvl]] – Lip – ''Chromobacterium viscosum''<br />
-	**[[1lgy]] – Lip II – ''Rhizopus niveus''<br />
	**[[1tic]] - Lip – ''Rhizopus oryzae''<br />		**[[1tic]] - Lip – ''Rhizopus oryzae''<br />
-	**[[1thg]] – Lip – ''Geotrichum candidum''<br />	+	**[[3tgl]], [[4tgl]], [[1tgl]] – RmLip – ''Rhyzomucor miehei''<br />
-	**[[3tgl]], [[4tgl]], [[1tgl]] – ~~RmLip–~~ ''Rhyzomucor miehei''<br />	+
	**[[2zvd]] – PsLip - ''Pseudomonas sp.'' – open state<br />		**[[2zvd]] – PsLip - ''Pseudomonas sp.'' – open state<br />
	**[[2z8x]] - PsLip – extracellular<br />		**[[2z8x]] - PsLip – extracellular<br />
Line 121:		Line 112:
	**[[4x71]], [[4x7b]], [[4x85]] – BstLip (mutant)<br />		**[[4x71]], [[4x7b]], [[4x85]] – BstLip (mutant)<br />
	**[[1ah7]] - Lip – ''Bacillus cereus''<br />		**[[1ah7]] - Lip – ''Bacillus cereus''<br />
-	**[[2qxt]], [[2qxu]], [[1isp]], [[1i6w]], [[4fdm]], [[5ct4]], [[5ct5]], [[5ct6]], [[5cri]] - BsLipA – ''Bacillus subtilis''<br />
-	**[[3d2a]], [[3d2b]], [[3d2c]], [[1t2n]], [[1t4m]], [[3qmm]], [[3qzu]], [[4fkb]], [[5ct8]], [[5ct9]], [[5cta]], [[5cur]], [[3qzu]], [[3qmm]] - BsLipA (mutant) <br />
	**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />		**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />
	**[[2z5g]], [[2dsn]] – GzLip T1 – ''Geobacillus zalihae''<br />		**[[2z5g]], [[2dsn]] – GzLip T1 – ''Geobacillus zalihae''<br />
Line 135:		Line 124:
	**[[5ah1]] – Lip – ''Clostridium botulinum''<br />		**[[5ah1]] – Lip – ''Clostridium botulinum''<br />
	**[[5ch8]] – Lip (mutant) – ''Penicillium cyclopium''<br />		**[[5ch8]] – Lip (mutant) – ''Penicillium cyclopium''<br />
		+
		+	*Bacterial lipase A
		+
		+	**[[3guu]] – CaLipA – ''Candida Antarctica''<br />
		+	**[[2veo]] – CaLipA – closed state<br />
		+	**[[2qua]], 2qub]] – SmLipA – ''Serratia marcescens''<br />
		+	**[[2qxt]], 2qxu]], 1isp]], 1i6w]], [[5ct4]], [5ct5]], [[5ct6]], [[5cri]] - BsLipA – ''Bacillus subtilis''<br />
		+	**[[3d2a]], 3d2b]], 3d2c]], 1t2n]], 1t4m]], [[5ct8]], [[5ct9]], [[5cta]], [[5cur]], [[3qzu]], [[3qmm]] - BsLipA (mutant) <br />
		+	**[[1r4z]] – BsLipA+Rc-IPG-phosphonate<br />
		+	**[[1r50]] – BsLipA +Sc-IPG-phosphonate<br />
		+
		+	*Bacterial lipase B
		+
		+	**[[4zv7]], [[3w9b]], [[5a6v]], [[5a71]], [[4k6g]], [[1tca]], [[1tcb]], [[1tcc]], [[1lbs]], [[1lbt]] – CaLipB <br />
		+	**[[3icv]], [[4k5q]], [[5k6h]], [[5k6k]] – CaLipB (mutant) <br />
		+	**[[5gv5]] - CaLipB + phosphonate<br />
		+	**[[3icw]] – CaLipB (mutant) + phosphonate<br />
		+	**[[5x7k]] – SmLipB NBD <br /><br />
		+
		+	*Bacterial lipase C
		+
		+	**[[5nen]] – SmLipC residues 1-443 <br />

	*Lipase/colipase complexes. The colipase is a co-enzyme whose binding to lipase optimizes the enzymatic activity		*Lipase/colipase complexes. The colipase is a co-enzyme whose binding to lipase optimizes the enzymatic activity
Line 171:		Line 182:
	**[[2nw6]] – BcLip+ S inhibitor <br />		**[[2nw6]] – BcLip+ S inhibitor <br />
	**[[4lip]], [[5lip]], [[1r4z]], [[1r50]] – BcLip+ Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate<br />		**[[4lip]], [[5lip]], [[1r4z]], [[1r50]] – BcLip+ Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate<br />
-	**[[1r4z]] – BsLipA +Rc-IPG-phosphonate <br />
-	**[[1r50]] - BsLipA +Sc-IPG-phosphonate <br />
	**[[1k8q]] - Lip+phosphonate – dog <br />		**[[1k8q]] - Lip+phosphonate – dog <br />
	**[[1ex9]] – Lip+Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate – ''Pseudomonas aeruginosa'' <br />		**[[1ex9]] – Lip+Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate – ''Pseudomonas aeruginosa'' <br />
	**[[5tgl]] – RmLip+N-hexyl-phosphonate <br />		**[[5tgl]] – RmLip+N-hexyl-phosphonate <br />
	**[[1lpb]] – pLip + colipase+C11 alkyl phosphonate <br />		**[[1lpb]] – pLip + colipase+C11 alkyl phosphonate <br />
-	**[[5gv5]] - CaLipB + phosphonate<br />
-	**[[3icw]] – CaLipB (mutant) + phosphonate<br />
	**[[3a70]] – PsLip+diethyl phosphate<br />		**[[3a70]] – PsLip+diethyl phosphate<br />
	**[[4glb]] – TlLip + nitrobenzaldehyde<br />		**[[4glb]] – TlLip + nitrobenzaldehyde<br />
Line 225:		Line 232:

	**[[3v9a]],[[3g9t]], [[3g9u]], [[3g9z]], [[3h19]], [[3h1a]], [[3h1b]], [[3l1h]], [[3l1i]], [[3l1j]], [[3fak]], [[3h17]], [[3h18]], [[3dnm]], [[3k6k]] - E/L - uncultured bacteria<br />		**[[3v9a]],[[3g9t]], [[3g9u]], [[3g9z]], [[3h19]], [[3h1a]], [[3h1b]], [[3l1h]], [[3l1i]], [[3l1j]], [[3fak]], [[3h17]], [[3h18]], [[3dnm]], [[3k6k]] - E/L - uncultured bacteria<br />
-	**[[1gz7]] - CrE/L <br />
	**[[3w9b]] - CaE/L <br />		**[[3w9b]] - CaE/L <br />
	**[[4v2i]] - E/L - ''Thalassospira''<br />		**[[4v2i]] - E/L - ''Thalassospira''<br />
Line 233:		Line 239:
	**[[4bzz]], [[4bzw]] - LpE/L <br />		**[[4bzz]], [[4bzw]] - LpE/L <br />
	**[[6gup]] - E/L - ''Aspergillus fumigatus''<br />		**[[6gup]] - E/L - ''Aspergillus fumigatus''<br />
		+	**[[1lgy]] – Lip2 – ''Rhizopus niveus''<br />
		+	**[[1gz7]] - CrLip2 <br />
		+	**[[4jei]] – Lip2 – ''Yarrowia lipolytica''<br />
		+	**[[1thg]] – Lip2 – ''Geotrichum candidum''<br />
	}}		}}
	==References==		==References==

Michal Harel at 08:37, 20 December 2018

Michal Harel — Thu, 20 Dec 2018 08:37:11 GMT

Michal Harel at 10:35, 25 October 2018

Michal Harel — Thu, 25 Oct 2018 10:35:31 GMT

←Older revision		Revision as of 10:35, 25 October 2018
Line 230:		Line 230:
	**[[4n5h]] - LrE/L (mutant) - ''Lactobacillus rhamnosus''<br />		**[[4n5h]] - LrE/L (mutant) - ''Lactobacillus rhamnosus''<br />
	**[[4n5i]] - LrE/L + inhibitor <br />		**[[4n5i]] - LrE/L + inhibitor <br />
-	**[[4ouk~~]], [[5po3~~]] - LrE/L (mutant) + inhibitor <br />	+	**[[4ouk]] - LrE/L (mutant) + inhibitor <br />
	**[[4bzz]], [[4bzw]] - LpE/L <br />		**[[4bzz]], [[4bzw]] - LpE/L <br />
	**[[6gup]] - E/L - ''Aspergillus fumigatus''<br />		**[[6gup]] - E/L - ''Aspergillus fumigatus''<br />

←Older revision		Revision as of 08:37, 20 December 2018
Line 118:		Line 118:
	**[[2w22]], [[6a12]] – GtLip – ''Geobacillus thermocatenulatus''<br />		**[[2w22]], [[6a12]] – GtLip – ''Geobacillus thermocatenulatus''<br />
	**[[5ce5]] – GtLip (mutant)<br />		**[[5ce5]] – GtLip (mutant)<br />
-	**[[1ji3]], [[1ku0]], [[4fmp]], [[4x6u]]– BstLip – ''Bacillus stearothermophilus''<br />	+	**[[1ji3]], [[1ku0]], [[4fmp]], [[4x6u]] – BstLip – ''Bacillus stearothermophilus''<br />
	**[[4x71]], [[4x7b]], [[4x85]] – BstLip (mutant)<br />		**[[4x71]], [[4x7b]], [[4x85]] – BstLip (mutant)<br />
	**[[1ah7]] - Lip – ''Bacillus cereus''<br />		**[[1ah7]] - Lip – ''Bacillus cereus''<br />
	**[[2qxt]], [[2qxu]], [[1isp]], [[1i6w]], [[4fdm]], [[5ct4]], [[5ct5]], [[5ct6]], [[5cri]] - BsLipA – ''Bacillus subtilis''<br />		**[[2qxt]], [[2qxu]], [[1isp]], [[1i6w]], [[4fdm]], [[5ct4]], [[5ct5]], [[5ct6]], [[5cri]] - BsLipA – ''Bacillus subtilis''<br />
-	**[[3d2a]], [[3d2b]], [[3d2c]], [[1t2n]], [[1t4m]], [[3qmm]], [[3qzu]], [[4fkb]], [[5ct8]], [[5ct9]], [[5cta]], [[5cur]] - ~~BsLip~~ (mutant) <br />	+	**[[3d2a]], [[3d2b]], [[3d2c]], [[1t2n]], [[1t4m]], [[3qmm]], [[3qzu]], [[4fkb]], [[5ct8]], [[5ct9]], [[5cta]], [[5cur]], [[3qzu]], [[3qmm]] - BsLipA (mutant) <br />
	**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />		**[[2ory]] – Lip – ''Photobacterium lypoliticum''<br />
	**[[2z5g]], [[2dsn]] – GzLip T1 – ''Geobacillus zalihae''<br />		**[[2z5g]], [[2dsn]] – GzLip T1 – ''Geobacillus zalihae''<br />
Line 171:		Line 171:
	**[[2nw6]] – BcLip+ S inhibitor <br />		**[[2nw6]] – BcLip+ S inhibitor <br />
	**[[4lip]], [[5lip]], [[1r4z]], [[1r50]] – BcLip+ Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate<br />		**[[4lip]], [[5lip]], [[1r4z]], [[1r50]] – BcLip+ Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate<br />
-	**[[1r4z]] – ~~BsLip~~+Rc-IPG-phosphonate <br />	+	**[[1r4z]] – BsLipA +Rc-IPG-phosphonate <br />
-	**[[1r50]] - ~~BsLip~~+Sc-IPG-phosphonate <br />	+	**[[1r50]] - BsLipA +Sc-IPG-phosphonate <br />
	**[[1k8q]] - Lip+phosphonate – dog <br />		**[[1k8q]] - Lip+phosphonate – dog <br />
	**[[1ex9]] – Lip+Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate – ''Pseudomonas aeruginosa'' <br />		**[[1ex9]] – Lip+Rc-(Rp,Sp)-1,2-dioctylcarbamoyl-glycero-3-O-phosphonate – ''Pseudomonas aeruginosa'' <br />